메뉴 건너뛰기




Volumn 275, Issue 2, 2008, Pages 263-270

Putative prion protein from Fugu (Takifugu rubripes)

Author keywords

Chaperone co expression; Fish prion protein; Nuclear magnetic resonance; Takifugu rubripes; Transmissible spongiform encephalopathy

Indexed keywords

CHAPERONE; GENE PRODUCT; GUANIDINE; POLYPEPTIDE; PRION PROTEIN; RECOMBINANT PROTEIN;

EID: 37849031495     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06196.x     Document Type: Article
Times cited : (8)

References (34)
  • 9
    • 33846476657 scopus 로고    scopus 로고
    • Novel aspects of prions, their receptor molecules, and innovative approaches for TSE therapy
    • Vana K, Zuber C, Nikles D Weiss S (2007) Novel aspects of prions, their receptor molecules, and innovative approaches for TSE therapy. Cell Mol Neurobiol 27, 107 128.
    • (2007) Cell Mol Neurobiol , vol.27 , pp. 107-128
    • Vana, K.1    Zuber, C.2    Nikles, D.3    Weiss, S.4
  • 11
    • 0037301562 scopus 로고    scopus 로고
    • An evolutionary basis for scrapie disease: Identification of a fish prion mRNA
    • Rivera-Milla E, Stürmer CA Málaga-Trillo E (2003) An evolutionary basis for scrapie disease: identification of a fish prion mRNA. Trends Genet 19, 72 75.
    • (2003) Trends Genet , vol.19 , pp. 72-75
    • Rivera-Milla, E.1    Stürmer, C.A.2    Málaga-Trillo, E.3
  • 12
    • 0037434837 scopus 로고    scopus 로고
    • Identification of cDNAs from Japanese pufferfish (Fugu rubripes) and Atlantic salmon (Salmo salar) coding for homologues to tetrapod prion proteins
    • Oidtmann B, Simon D, Holtkamp N, Hoffmann R Baier M (2003) Identification of cDNAs from Japanese pufferfish (Fugu rubripes) and Atlantic salmon (Salmo salar) coding for homologues to tetrapod prion proteins. FEBS Lett 538, 96 100.
    • (2003) FEBS Lett , vol.538 , pp. 96-100
    • Oidtmann, B.1    Simon, D.2    Holtkamp, N.3    Hoffmann, R.4    Baier, M.5
  • 13
    • 8444247483 scopus 로고    scopus 로고
    • Evolution of vertebrate genes related to prion and Shadoo proteins - Clues from comparative genomic analysis
    • Premzl M, Gready JE, Jermiin LS, Simonic T Marshall Graves JA (2004) Evolution of vertebrate genes related to prion and Shadoo proteins - clues from comparative genomic analysis. Mol Biol Evol 21, 2210 2231.
    • (2004) Mol Biol Evol , vol.21 , pp. 2210-2231
    • Premzl, M.1    Gready, J.E.2    Jermiin, L.S.3    Simonic, T.4    Marshall Graves, J.A.5
  • 14
    • 12544259444 scopus 로고    scopus 로고
    • Molecular characterization, phylogenetic relationships, and developmental expression patterns of prion genes in zebrafish (Danio rerio)
    • Cotto E, Andre M, Forgue J, Fleury HJ Babin PJ (2005) Molecular characterization, phylogenetic relationships, and developmental expression patterns of prion genes in zebrafish (Danio rerio). FEBS J 272, 500 513.
    • (2005) FEBS J , vol.272 , pp. 500-513
    • Cotto, E.1    Andre, M.2    Forgue, J.3    Fleury, H.J.4    Babin, P.J.5
  • 16
    • 33846844874 scopus 로고    scopus 로고
    • Comparative genomic analysis of prion genes
    • Premzl M Gamulin V (2007) Comparative genomic analysis of prion genes. BMC Genomics 8, 1.
    • (2007) BMC Genomics , vol.8 , pp. 1
    • Premzl, M.1    Gamulin, V.2
  • 18
    • 23944502484 scopus 로고    scopus 로고
    • Cloning and characterization of prion protein coding genes of Japanese seabass (Lateolabrax japonicus) and Japanese flounder (Paralichthys olivaceus)
    • Liao M, Zhang Z, Yang G, Sun X, Zou G, Wei Q Wang D (2005) Cloning and characterization of prion protein coding genes of Japanese seabass (Lateolabrax japonicus) and Japanese flounder (Paralichthys olivaceus). Aquaculture 249, 47 53.
    • (2005) Aquaculture , vol.249 , pp. 47-53
    • Liao, M.1    Zhang, Z.2    Yang, G.3    Sun, X.4    Zou, G.5    Wei, Q.6    Wang, D.7
  • 21
    • 2442707716 scopus 로고    scopus 로고
    • Fugu genome analysis provides evidence for a whole-genome duplication early during the evolution of ray-finned fishes
    • Christoffels A, Koh EG, Chia JM, Brenner S, Aparicio S Venkatesh B (2004) Fugu genome analysis provides evidence for a whole-genome duplication early during the evolution of ray-finned fishes. Mol Biol Evol 21, 1146 1151.
    • (2004) Mol Biol Evol , vol.21 , pp. 1146-1151
    • Christoffels, A.1    Koh, E.G.2    Chia, J.M.3    Brenner, S.4    Aparicio, S.5    Venkatesh, B.6
  • 22
    • 1242274629 scopus 로고    scopus 로고
    • Major events in the genome evolution of vertebrates: Paranome age and size differ considerably between ray-finned fishes and land vertebrates
    • Vandepoele K, De Vos W, Taylor JS, Meyer A Van de Peer Y (2004) Major events in the genome evolution of vertebrates: paranome age and size differ considerably between ray-finned fishes and land vertebrates. Proc Natl Acad Sci USA 101, 1638 1643.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1638-1643
    • Vandepoele, K.1    De Vos, W.2    Taylor, J.S.3    Meyer, A.4    Van De Peer, Y.5
  • 24
    • 4043053590 scopus 로고    scopus 로고
    • Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy
    • Lysek DA Wüthrich K (2004) Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy. Biochemistry 43, 10393 10399.
    • (2004) Biochemistry , vol.43 , pp. 10393-10399
    • Lysek, D.A.1    Wüthrich, K.2
  • 25
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
    • Nishihara K, Kanemori M, Kitagawa M, Yanagi H Yura T (1998) Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl Environ Microbiol 64, 1694 1699.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 26
    • 0034050548 scopus 로고    scopus 로고
    • Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli
    • Nishihara K, Kanemori M, Yanagi H Yura T (2000) Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl Environ Microbiol 66, 884 889.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 884-889
    • Nishihara, K.1    Kanemori, M.2    Yanagi, H.3    Yura, T.4
  • 27
    • 0029989229 scopus 로고    scopus 로고
    • Expression of correctly folded proteins in Escherichia coli
    • Georgiou G Valax P (1996) Expression of correctly folded proteins in Escherichia coli. Curr Opin Biotechnol 7, 190 197.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 190-197
    • Georgiou, G.1    Valax, P.2
  • 28
    • 0032409445 scopus 로고    scopus 로고
    • Sequence properties of GPI-anchored proteins near the omega-site: Constraints for the polypeptide binding site of the putative transamidase
    • Eisenhaber B, Bork P Eisenhaber F (1998) Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase. Protein Eng 11, 1155 1161.
    • (1998) Protein Eng , vol.11 , pp. 1155-1161
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 29
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding
    • Zahn R, von Schroetter C Wüthrich K (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett 417, 400 404.
    • (1997) FEBS Lett , vol.417 , pp. 400-404
    • Zahn, R.1    Von Schroetter, C.2    Wüthrich, K.3
  • 30
    • 0032568592 scopus 로고    scopus 로고
    • A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH
    • Hornemann S Glockshuber R (1998) A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc Natl Acad Sci USA 95, 6010 6014.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6010-6014
    • Hornemann, S.1    Glockshuber, R.2
  • 31
    • 0038266598 scopus 로고    scopus 로고
    • Atypical effect of salts on the thermodynamic stability of human prion protein
    • Apetri AC Surewicz WK (2003) Atypical effect of salts on the thermodynamic stability of human prion protein. J Biol Chem 278, 22187 22192.
    • (2003) J Biol Chem , vol.278 , pp. 22187-22192
    • Apetri, A.C.1    Surewicz, W.K.2
  • 32
    • 0037007448 scopus 로고    scopus 로고
    • Folding and intrinsic stability of deletion variants of PrP(121-231), the folded C-terminal domain of the prion protein
    • Eberl H Glockshuber R (2002) Folding and intrinsic stability of deletion variants of PrP(121-231), the folded C-terminal domain of the prion protein. Biophys Chem 96, 293 303.
    • (2002) Biophys Chem , vol.96 , pp. 293-303
    • Eberl, H.1    Glockshuber, R.2
  • 33
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82, 70 77.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 34
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM Bolen DW (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063 8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.